CHRC1_HUMAN
ID CHRC1_HUMAN Reviewed; 131 AA.
AC Q9NRG0;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Chromatin accessibility complex protein 1;
DE Short=CHRAC-1;
DE AltName: Full=Chromatin accessibility complex 15 kDa protein;
DE Short=CHRAC-15;
DE Short=HuCHRAC15;
DE AltName: Full=DNA polymerase epsilon subunit p15;
GN Name=CHRAC1; Synonyms=CHRAC15;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE CHRAC ISWI CHROMATIN
RP REMODELING COMPLEX, INTERACTION WITH SMARCA5; BAZ1A AND POLE3, AND TISSUE
RP SPECIFICITY.
RX PubMed=10880450; DOI=10.1093/emboj/19.13.3377;
RA Poot R.A., Dellaire G., Huelsmann B.B., Grimaldi M.A., Corona D.F.V.,
RA Becker P.B., Bickmore W.A., Varga-Weisz P.D.;
RT "HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two
RT novel histone-fold proteins.";
RL EMBO J. 19:3377-3387(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH BAZ1A.
RX PubMed=12434153; DOI=10.1038/ng1046;
RA Collins N., Poot R.A., Kukimoto I., Garcia-Jimenez C., Dellaire G.,
RA Varga-Weisz P.D.;
RT "An ACF1-ISWI chromatin-remodeling complex is required for DNA replication
RT through heterochromatin.";
RL Nat. Genet. 32:627-632(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH SMARCA5 AND BAZ1A.
RX PubMed=14759371; DOI=10.1016/s1097-2765(03)00523-9;
RA Kukimoto I., Elderkin S., Grimaldi M., Oelgeschlager T., Varga-Weisz P.D.;
RT "The histone-fold protein complex CHRAC-15/17 enhances nucleosome sliding
RT and assembly mediated by ACF.";
RL Mol. Cell 13:265-277(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Forms a complex with DNA polymerase epsilon subunit POLE3 and
CC binds naked DNA, which is then incorporated into chromatin, aided by
CC the nucleosome remodeling activity of ISWI/SNF2H and ACF1. Does not
CC enhance nucleosome sliding activity of the ACF-5 ISWI chromatin
CC remodeling complex (PubMed:14759371). {ECO:0000269|PubMed:14759371}.
CC -!- SUBUNIT: Heterodimer with POLE3; binds to DNA (PubMed:10880450).
CC Component of the CHRAC ISWI chromatin remodeling complex at least
CC composed of SMARCA5/SNF2H, BAZ1A/ACF1, CHRAC1 and POLE3; the complex
CC preferentially binds DNA through the CHRAC1-POLE3 heterodimer and
CC possesses ATP-dependent nucleosome-remodeling activity
CC (PubMed:10880450). Within the complex, the heterodimer with POLE3
CC interacts with SMARCA5/SNF2H; the interaction is direct and enhances
CC nucleosome sliding activity by the SMARCA5/SNF2H and BAZ1A/ACF1
CC interaction (PubMed:10880450, PubMed:14759371). Within the complex, the
CC heterodimer with POLE3 interacts with BAZ1A/ACF1; the interactions are
CC direct (PubMed:10880450, PubMed:12434153, PubMed:14759371).
CC {ECO:0000269|PubMed:10880450, ECO:0000269|PubMed:12434153,
CC ECO:0000269|PubMed:14759371}.
CC -!- INTERACTION:
CC Q9NRG0; Q8IZU0: FAM9B; NbExp=7; IntAct=EBI-2795492, EBI-10175124;
CC Q9NRG0; Q9NRF9: POLE3; NbExp=13; IntAct=EBI-2795492, EBI-744901;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10880450}.
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DR EMBL; AF226076; AAF72416.1; -; mRNA.
DR EMBL; AK023537; BAB14601.1; -; mRNA.
DR EMBL; BC015891; AAH15891.1; -; mRNA.
DR CCDS; CCDS6379.1; -.
DR RefSeq; NP_059140.1; NM_017444.5.
DR AlphaFoldDB; Q9NRG0; -.
DR SMR; Q9NRG0; -.
DR BioGRID; 119904; 61.
DR ComplexPortal; CPX-785; CHRAC chromatin remodeling complex.
DR CORUM; Q9NRG0; -.
DR IntAct; Q9NRG0; 9.
DR MINT; Q9NRG0; -.
DR STRING; 9606.ENSP00000220913; -.
DR GlyGen; Q9NRG0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NRG0; -.
DR PhosphoSitePlus; Q9NRG0; -.
DR BioMuta; CHRAC1; -.
DR DMDM; 22653683; -.
DR EPD; Q9NRG0; -.
DR jPOST; Q9NRG0; -.
DR MassIVE; Q9NRG0; -.
DR MaxQB; Q9NRG0; -.
DR PaxDb; Q9NRG0; -.
DR PeptideAtlas; Q9NRG0; -.
DR PRIDE; Q9NRG0; -.
DR ProteomicsDB; 82351; -.
DR TopDownProteomics; Q9NRG0; -.
DR Antibodypedia; 27623; 192 antibodies from 29 providers.
DR DNASU; 54108; -.
DR Ensembl; ENST00000220913.10; ENSP00000220913.5; ENSG00000104472.10.
DR GeneID; 54108; -.
DR KEGG; hsa:54108; -.
DR MANE-Select; ENST00000220913.10; ENSP00000220913.5; NM_017444.6; NP_059140.1.
DR UCSC; uc003yvl.4; human.
DR CTD; 54108; -.
DR DisGeNET; 54108; -.
DR GeneCards; CHRAC1; -.
DR HGNC; HGNC:13544; CHRAC1.
DR HPA; ENSG00000104472; Low tissue specificity.
DR MIM; 607268; gene.
DR neXtProt; NX_Q9NRG0; -.
DR OpenTargets; ENSG00000104472; -.
DR PharmGKB; PA26481; -.
DR VEuPathDB; HostDB:ENSG00000104472; -.
DR eggNOG; KOG1657; Eukaryota.
DR GeneTree; ENSGT00510000048543; -.
DR HOGENOM; CLU_045277_11_2_1; -.
DR InParanoid; Q9NRG0; -.
DR OMA; DHSENEA; -.
DR OrthoDB; 1622159at2759; -.
DR PhylomeDB; Q9NRG0; -.
DR TreeFam; TF350392; -.
DR PathwayCommons; Q9NRG0; -.
DR SignaLink; Q9NRG0; -.
DR BioGRID-ORCS; 54108; 24 hits in 1084 CRISPR screens.
DR ChiTaRS; CHRAC1; human.
DR GenomeRNAi; 54108; -.
DR Pharos; Q9NRG0; Tbio.
DR PRO; PR:Q9NRG0; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NRG0; protein.
DR Bgee; ENSG00000104472; Expressed in epithelial cell of pancreas and 147 other tissues.
DR ExpressionAtlas; Q9NRG0; baseline and differential.
DR Genevisible; Q9NRG0; HS.
DR GO; GO:0008623; C:CHRAC; IBA:GO_Central.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; NAS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006334; P:nucleosome assembly; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; DNA-binding; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..131
FT /note="Chromatin accessibility complex protein 1"
FT /id="PRO_0000089656"
FT REGION 109..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..124
FT /evidence="ECO:0000255"
FT COMPBIAS 114..131
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT VARIANT 55
FT /note="C -> Y (in dbSNP:rs2231522)"
FT /id="VAR_013755"
FT VARIANT 126
FT /note="H -> R (in dbSNP:rs2231524)"
FT /id="VAR_013756"
SQ SEQUENCE 131 AA; 14711 MW; BC58A99CF58ACF74 CRC64;
MADVVVGKDK GGEQRLISLP LSRIRVIMKS SPEVSSINQE ALVLTAKATE LFVQCLATYS
YRHGSGKEKK VLTYSDLANT AQQSETFQFL ADILPKKILA SKYLKMLKEE KREEDEENDN
DNESDHDEAD S
